2bjj

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2bjj, resolution 2.40Å

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STRUCTURE OF RECOMBINANT HUMAN LACTOFERRIN PRODUCED IN THE MILK OF TRANSGENIC COWS

Overview

Human lactoferrin (hLF) is an iron-binding glycoprotein involved in the, host defence against infection and excessive inflammation. As the, availability of (human milk-derived) natural hLF is limited, alternative, means of production of this biopharmaceutical are extensively researched., Here we report the crystal structure of recombinant hLF (rhLF) expressed, in the milk of transgenic cows at a resolution of 2.4 A. To our knowledge, the first reported structure of a recombinant protein produced in milk of, transgenic livestock. Even though rhLF contains oligomannose- and, hybrid-type N-linked glycans next to complex-type glycans, which are the, only glycans found on natural hLF, the structures are identical within the, experimental error (r.m.s. deviation of only 0.28 A for the main-chain, atoms). Of the differences in polymorphic amino acids between the natural, and rhLF variant used, only the side-chain of Asp561 could be modeled into, the rhLF electron density map. Taken together, the results confirm the, structural integrity of the rhLF variant used in this study. It also, confirms the validity of the transgenic cow mammary gland as a vehicle to, produce recombinant human proteins.

About this Structure

2BJJ is a Single protein structure of sequence from Homo sapiens with NAG, FE and CO3 as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin., Thomassen EA, van Veen HA, van Berkel PH, Nuijens JH, Abrahams JP, Transgenic Res. 2005 Aug;14(4):397-405. PMID:16201406

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